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Glutathione Peroxidase, V. The kinetic mechanism
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“During the enzymatic reduction of hydrogen peroxide, Sec undergoes sequential oxidation by hydrogen peroxide to form a selenenic acid, Se-OH, followed by reaction with GSH to form a Se-SG intermediate before a second GSH combines to form GSSG, resolving the active site to Se-H (133, 278).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [133]
Citations
Cites
Chem in Biochem Gue - roult Enzymol / this Biochim
Boivin (1969) · BioL Clin BioL Chem Biochem J Biophys Acta
UnresolvedUsing the terminology of Clelandt this mecha - Klin Wochemchr Biochim / Lab Clin
Flohe (1971) · Biophys Acta
UnresolvedChim Brit
Necheles (1970) · Acta J Haematol
Unresolved
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Items 301–341 of 341
Lv, S., Zheng, Q., Mu, Y., et al. (2007) · Journal of Inclusion Phenomena and Macrocyclic Chemistry · doi:10.1007/s10847-007-9362-8 · Cited by 4
Yin, Y., Lang, C., Hu, X., et al. (2014) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162014010142 · Cited by 4
Antioxidant status and clinicopathological parameters in patients with Parkinson's disease
Vukajlović, J. M., Pejić, S., Todorović, A., Šobot, A. V., Drakulić, D., Pavlović, I., Stefanović, A., Prostran, M. S., Ilic, T. V., & Stojanov, M. (2018) · Vojnosanitetski pregled · doi:10.2298/vsp180718148m · Cited by 4
Li, J., Jia, W., Ma, G., Zhang, X., An, S., Wang, T., & Shi, S. (2020) · Organic & Biomolecular Chemistry · doi:10.1039/d0ob00122h · Cited by 4
Helmut Sies and the compartmentation of hydroperoxide metabolism
Flohé, L. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.11.018 · Cited by 4
Self-citationBrain Insulin Resistance: Focus on Insulin Receptor-Mitochondria InteractionsPreprint
Pinelis, I., & Pinelis, V. G. (2021) · Preprints.org · doi:10.20944/preprints202103.0401.v1 · Cited by 3
Redox Pioneer: Professor Leopold Flohé
Ursini, F., & Maiorino, M. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3192 · Cited by 3
Engineering Peptidyl and Protein Glutathione Peroxidase Mimics
Delsuc, N. (2023) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789811261664_0006 · Cited by 2
Pathogenesis-guided nanozymes: from design to therapy for gastrointestinal inflammation
Du, Y., He, Z., Chen, C., et al. (2025) · MedMat. · doi:10.1097/mm9.0000000000000037 · Cited by 2
A Systems Biology Approach Towards a Comprehensive Understanding of Ferroptosis
Arbatskiy, M. S., Balandin, D. E., Akberdin, I. R., & Churov, A. V. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252111782 · Cited by 4
Characterization of several members of the thiol oxidoreductase family
Varlamova, E. G., Goltyaev, M. V., Novoselov, S. V., Novoselov, V. I., & Fesenko, E. E. (2013) · Molecular Biology · doi:10.1134/s0026893313040146 · Cited by 2
Artificial Enzyme Construction with Temperature Sensitivity
Lin, T., Lin, J., Huang, X., et al. (2011) · Communications in computer and information science · doi:10.1007/978-3-642-23321-0_40 · Cited by 2
Shamberger, R. J. (1983) · Springer eBooks · doi:10.1007/978-1-4684-4313-4_1 · Cited by 2
Turell, L., Möller, M. N., Orrico, F., Randall, L. M., Steglich, M., Villar, S. F., Denicola, A., & Thomson, L. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-90219-9.00025-x · Cited by 3
Sulfur and the Metabolism of Xenobiotics
Lafranconi, W. M. (1986) · Springer eBooks · doi:10.1007/978-1-4757-9438-0_9 · Cited by 2
Se and Non-Se Glutathione Peroxidases: Enzymology and Cell Physiology
Sies, H., Wendel, A., & Burk, R. F. (1982) · Elsevier eBooks · doi:10.1016/b978-0-08-024421-1.50012-4 · Cited by 2
Bajpai, S., & Behera, R. N. (2025) · Asian Journal of Organic Chemistry · doi:10.1002/ajoc.202400717 · Cited by 1
Pavliuk, A., Івасів, В. В., & Nebesnyi, R. (2025) · Chemistry & Chemical Technology · doi:10.23939/chcht19.01.117 · Cited by 1
The physiological role of peroxiredoxin 2 in human erythrocytes: a kinetic analysis
Benfeitas, R. (2011) · Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) · Cited by 1
Prasad, A. S. (1978) · Springer eBooks · doi:10.1007/978-1-4684-0793-8_9 · Cited by 1
Reactive Oxygen Species-Toxicity, Metabolism, and Reactions in the Eye
Buckley, B., & Freeman, B. Α. (1987) · Cell and developmental biology of the eye · doi:10.1007/978-1-4612-4784-5_6 · Cited by 1
Untersuchungen zur Rolle der Glutathion-Peroxidase 4 als möglicher Redox-Sensor in Säugetierzellen
Grünler, N. (2015) · Site cant be reached · doi:10.5282/edoc.18272
Januel, C., & de Biochimie, D. (2003) · OpenGrey (Institut de l'Information Scientifique et Technique)
Effect of air, peroxides and diabetes on antioxidant enzyme localization in red blood cells
Stoyanova, Z. (2013) · Spectrum Research Repository (Concordia University)
Jiao, S. F., Yin, Y. Z., Gan, X., et al. (2014) · Advanced materials research · doi:10.4028/www.scientific.net/amr.926-930.230
Yin, Y. Z., Jiao, S. F., Gan, X., et al. (2014) · Advanced materials research · doi:10.4028/www.scientific.net/amr.940.20
Scimeca, M. S. (2005) · eCommons (Cornell University)
Cyclodextrin-based Mimics of Selenoproteins
Yan, F., & Luo, G. (2011) · Advanced topics in science and technology in China · doi:10.1007/978-3-642-22236-8_15
Differential Regulation and Function of Glutathione Peroxidases and Other Selenoproteins
Lei, X. G. (2001) · Modern nutrition · doi:10.1201/9781420039108.ch17
A novel micromolecule glutathione peroxidase mimic
Chang-cheng, G., Zou, X.-F., Wu, Q., et al. (2011) · IEEE International Symposium on IT in Medicine and Education (ITME) · doi:10.1109/itime.2011.6132096
“The assay of kinetics of synthesized peptide was similar to that for native GPX [15].”
ResultDetermination of selenium in selenium enriched yeast.
Kennedy, K. M. (1999) · Research@THEA
Selenium-Containing Catalysts Encapsulated in Protein Systems
Pan, T., & Liu, J. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803836-9.00006-7
Doser les enzymes du stress oxydant, oui ou non ?
Baudin, B. (2020) · Revue Francophone des Laboratoires · doi:10.1016/s1773-035x(20)30164-7
Free Flavin Participates in Iron and Also Oxygen Metabolism in Bacteria
Suzuki, T., Kimata, S., Satoh, J., et al. (2020) · Institutional Repositories DataBase (IRDB)
Pawlak, A. L. (1974) · Journal of Molecular Medicine · doi:10.1007/bf01468801
(2006) · Springer eBooks · doi:10.1007/3-540-37704-2_25
Maker, H. S. (1983) · Springer eBooks · doi:10.1007/978-1-4684-4367-7_22
Spector, L. B. (1982) · Springer eBooks · doi:10.1007/978-1-4612-5663-2_2
Behera, R. N., Bajpai, S., & Daipule, K. (2023) · SSRN Electronic Journal · doi:10.2139/ssrn.4482094
Nanoenzymes as Selenoprotein Mimics
Huang, X., Yin, X., Xu, J., & Liu, J. (2011) · Advanced topics in science and technology in China · doi:10.1007/978-3-642-22236-8_19
Metadata
- Authors
- Flohé, L., Loschen, G., Günzler, W. A., & Eichele, E.
- ORCID
- Flohé, Leopold
- Venue
- Hoppe-Seyler´s Zeitschrift für physiologische Chemie
- Publisher
- Walter de Gruyter GmbH
- Published
- 1972-01
- Volume
- 353
- Issue
- 1
- Pages
- 987-1000
- ISSN
- 0018-4888 (ISSN-L)
- OpenAlex
- W2002449018
- Cited by
- 340
- References
- 3
- Citations by year
- 2025: 4 · 2024: 5 · 2023: 7 · 2022: 4 · 2021: 5 · 2020: 11 · 2019: 5 · 2018: 3 · 2017: 6 · 2016: 4 · 2015: 10 · 2014: 13 · 2013: 11 · 2012: 6
- FWCI
- 4.47
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Hoppe-Seyler´s Zeitschrift für physiologische Chemie (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- glutathione peroxidase, enzyme kinetics, kinetic mechanism, hydrogen peroxide reduction, glutathione
- MeSH terms
- Animals, Cattle, Chemistry, Physical, Coumarins, Enzyme Activation, Glutathione, Hydrogen-Ion Concentration, Kinetics, Mathematics, Oxidation-Reduction, Peroxidases, Peroxides, Polarography, Spectrophotometry, Sulfates, Sulfhydryl Compounds, Titanium
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